ID   CBIT_SALTI              Reviewed;         192 AA.
AC   Q8Z5M9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating);
DE            EC=2.1.1.196;
GN   Name=cbiT; OrderedLocusNames=STY2235, t0844;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Catalyzes the methylation of C-15 in cobalt-precorrin-6B
CC       followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 +
CC         CO2 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36067,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:70791, ChEBI:CHEBI:72780; EC=2.1.1.196;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 8/10.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Bacterial-
CC       type CbiT family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD02391.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68531.1; -; Genomic_DNA.
DR   RefSeq; NP_456581.1; NC_003198.1.
DR   RefSeq; WP_000650991.1; NZ_WSUR01000002.1.
DR   AlphaFoldDB; Q8Z5M9; -.
DR   SMR; Q8Z5M9; -.
DR   STRING; 220341.16503262; -.
DR   EnsemblBacteria; AAO68531; AAO68531; t0844.
DR   KEGG; stt:t0844; -.
DR   KEGG; sty:STY2235; -.
DR   PATRIC; fig|220341.7.peg.2254; -.
DR   eggNOG; COG2242; Bacteria.
DR   HOGENOM; CLU_094143_0_0_6; -.
DR   OMA; RCKFVYA; -.
DR   UniPathway; UPA00148; UER00229.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0043776; F:cobalt-precorrin-6B C5-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02469; CbiT; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..192
FT                   /note="Cobalt-precorrin-6B C(15)-methyltransferase
FT                   (decarboxylating)"
FT                   /id="PRO_0000134948"
FT   BINDING         15
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..43
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  20774 MW;  9D650C5D2DDF0258 CRC64;
     MKDELFLRGE NVPMTKEAVR ALALSKLELH RASHLIDVGA GTGSVSIEAA LQFPSLQVTA
     IERNPAALRL LDENRQRFAC GNIDILPGEA PMTITGKADA VFMGGSGGHL TALIDWAMGH
     LHPGGRLVMT FILQENLHSA LAHLVHIGAC RMDCVQLQLS SLTPLGAGHY FKPNNPVFVI
     ACQKEENHVR DI